High impact information on ARL3

• Furthermore, Arl3 co-purified with microtubules from bovine brain [1].
• In contrast, cofactor C and Arl3 localized predominantly to the photoreceptor connecting cilium in rod and cone photoreceptors [1].
• In this study we have examined the relationship between RP2, cofactor C and Arl3 in patient-derived cell lines and in the retina [1].
• Arl3 behaved as a microtubule-associated protein: it co-localized with microtubules in HeLa cells and this was enhanced following microtubule stabilization with taxol [1].
• Following microtubule depolymerization with nocodazole, Arl3 relocalized to the nuclear membrane [1].

Biological context of ARL3

• Two-hybrid screens of human cDNA libraries with dominant active mutants of human ARL1, ARL2, and ARL3 identified eight different but overlapping sets of binding partners [2].
• CONCLUSION: The disturbed magnesium binding site and the independence of GDP coordination from the presence of Mg2+ separate ARL2 and ARL3 from Arf proteins [3].
• Here we describe the methodologies that we have developed to analyze the interaction of RP2 with Arl3 and to investigate the effect of RP2 post-translational modifications on its subcellular and tissue localization [4].
• We conclude that Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis [5].
• Somewhat paradoxically, no phenotypes were observed Arl2 expression was knocked down or Arl3 activity was increased in HeLa cells [5].

Anatomical context of ARL3

• These data suggest that RP2 functions in concert with Arl3 to link the cell membrane with the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery [1].
• The presence of Arl3 in centrosomes, mitotic spindles, midzones, midbodies, and cilia are all supportive of roles in microtubule-dependent processes [5].
• A number of human tumor cell lines expressed Arl3, as determined by immunoblotting with an Arl-specific antibody, raised against a peptide derived from the human Arl3 sequence [6].

Associations of ARL3 with chemical compounds

• In contrast to ARF proteins, the Arl3 protein has reduced dependence on phospholipids and magnesium for guanine nucleotide exchange [6].
• The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner [7].

Physical interactions of ARL3

• It has been shown that RP2 can interact directly with Arl3 [4].

Other interactions of ARL3

• Two recent papers show that the Arl3p and Arl1p small GTPases act sequentially to recruit GRIP domain proteins to the Golgi [8].
• Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3 [9].
• The small G protein-encoding LdARL-3A gene, a homologue of the human ARL-3 gene, was isolated from Leishmania donovani, and its protein product characterised [10].
• Genes downregulated in spheroids were: (5) phosphoglycerate kinase; (6) ARL-3, a ras-related GTP binding protein; (7) MHC class III complement 4A; and (8) 2,4-dienoyl-CoA [11].

Analytical, diagnostic and therapeutic context of ARL3

• Assignment of the human ADP-ribosylation factor-like 3 (ARL3) gene to chromosome 10 band q23.3 by radiation hybrid mapping [12].
• Northern blots of mRNA from seven human tissues and four rat tissues revealed the presence of a ubiquitous band of about 1 kilobase in length that hybridized with the corresponding Arl3 probes [6].

References